BMRB Entry 30866

Name: Structure of the cryptic HMA domain of the human copper transporter ATP7A
Published: 2021-09-07

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PDB ID: 7lu8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30866
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of the cryptic HMA domain of the human copper transporter ATP7A PubMed: 34461106

Deposition date: 2021-02-21 Original release date: 2021-09-07

Authors: Lee, W.; Uhlemann, E.; Tonelli, M.; Dmitriev, O.

Citation: Uhlemann, E.; Lee, W.; Tonelli, M.; Dmitriev, O.. "At sixes and sevens: a cryptic domain in the metal binding chain of the human copper transporter ATP7A" Biophys. J. 120, 4600-4607 (2021).

Assembly members:
entity_1, polymer, 76 residues, 8367.748 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTYB12

Entity Sequences (FASTA):
entity_1: AGHMTDTLFLTVTASLTLPW DHIQSTLLKTKGVTDIKIYP QKRTVAVTIIPSIVNANQIK ELVPELSLDTGTLEKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	141
15N chemical shifts	66
1H chemical shifts	66

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 76 residues - 8367.748 Da.

1

ALA

GLY

HIS

MET

THR

ASP

THR

LEU

PHE

LEU

2

THR

VAL

THR

ALA

SER

LEU

THR

LEU

PRO

TRP

3

ASP

HIS

ILE

GLN

SER

THR

LEU

LYS

THR

4

LYS

GLY

VAL

THR

ASP

ILE

LYS

ILE

TYR

PRO

5

GLN

LYS

ARG

THR

VAL

ALA

VAL

THR

ILE

6

PRO

SER

ILE

VAL

ASN

ALA

ASN

GLN

ILE

LYS

7

GLU

LEU

VAL

PRO

GLU

LEU

SER

LEU

ASP

THR

8

GLY

THR

LEU

GLU

LYS

Samples:

sample_1: HMA2A, [U-13C; U-15N], 0.35 ± 0.02 mM; HEPES 50 ± 1 mM; sodium chloride 150 ± 1 mM; TCEP 5 ± 0.2 mM

sample_conditions_1: ionic strength: 210 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

VNMR, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

APES, Lee - peak picking

NMRFAM-SPARKY, Lee, Tonelli, Markley - chemical shift assignment

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation

PONDEROSA-C/S, Lee, Stark, Markley - structure calculation

AUDANA, Lee, Petit, Cornilescu, Stark, Markley - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker AVANCE III 900 MHz
Varian Uniform NMR System 600 MHz
Bruker AVANCE III 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts